MS116_CANAL
ID MS116_CANAL Reviewed; 668 AA.
AC Q5APM7; A0A1D8PEF1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ATP-dependent RNA helicase MSS116, mitochondrial;
DE EC=3.6.4.13;
DE Flags: Precursor;
GN Name=MSS116; OrderedLocusNames=CAALFM_C108810CA;
GN ORFNames=CaO19.12201, CaO19.4739;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
CC -!- FUNCTION: ATP-dependent RNA helicase required for mitochondrial
CC splicing of group I and II introns. Also required for efficient
CC mitochondrial translation (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1
CC subfamily. {ECO:0000305}.
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DR EMBL; CP017623; AOW26518.1; -; Genomic_DNA.
DR RefSeq; XP_723426.2; XM_718333.2.
DR AlphaFoldDB; Q5APM7; -.
DR SMR; Q5APM7; -.
DR STRING; 237561.Q5APM7; -.
DR GeneID; 3634792; -.
DR KEGG; cal:CAALFM_C108810CA; -.
DR CGD; CAL0000195117; MSS116.
DR VEuPathDB; FungiDB:C1_08810C_A; -.
DR eggNOG; KOG0342; Eukaryota.
DR HOGENOM; CLU_003041_26_6_1; -.
DR InParanoid; Q5APM7; -.
DR OrthoDB; 537587at2759; -.
DR PRO; PR:Q5APM7; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Mitochondrion; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Reference proteome; RNA-binding;
KW Transit peptide; Translation regulation.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 39..668
FT /note="ATP-dependent RNA helicase MSS116, mitochondrial"
FT /id="PRO_0000294628"
FT DOMAIN 119..300
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 332..501
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 585..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 87..115
FT /note="Q motif"
FT MOTIF 242..245
FT /note="DEAD box"
FT COMPBIAS 587..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 668 AA; 76701 MW; 472751647F0D67CB CRC64;
MLKQLSRSLG IRSSPIVANL IRSKQVCTRG FHISLVKQNT SSKVNEITDI TSDSLKVKED
AAGSDLPSTK TDKKSKSESF QPVKFEDFKG KGYIHDSIIN SLHKNDFKEL TPIQQKSLVP
IFNTEKGLVC RAKTGTGKTL AFAVPTLQYA YKNRGKGVST VVLVPTRDLA FQIEEEYRKL
ISHLKYNERP NLELIIGGQR TSFNPRRPAE IVIATPGRLE KELQTDRKLA KCFSNVTYRI
YDEADRLLDV GFESVLNEID GLLYKVRTTP KPIKSLLFSA TVDEAISEFS KKHIHPEYEF
LNTVTKDDLE IPENIHQQLI ECTDGIDKVN VSLSELHGIM KQHNDYKVIV FLPTKTAVDW
FYEYITNALD DELFELFSKP PRVFMLHGGR SVRQRSAALK GFKVAKKGIL ISTDVAARGI
DVKDVTNVMQ MFPSVEIADY IHKVGRTGRA GKKGKASLFA TPAELPYVSL LKRKRKVKFQ
EVIQSEKLNS SNIIDQIESP LDSTKEFLAT MVGYLQQLQS AHRLDYDSLV IENMELYRKL
VRDDKAMLES RILSRIGKGI SAHVKRRYFT RTRYQSHDDA EFDSYSDFSR SGMSQRPRSN
DRSSKMTFNG RGKYGNNRNN DWSYQNKNRY NNNNNRQTER SYDSDRKSHN DWKYEKKFEH
RRIRDHDE
